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Database: PDB
Entry: 2QDJ
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HEADER    ANTITUMOR PROTEIN                       21-JUN-07   2QDJ              
TITLE     CRYSTAL STRUCTURE OF THE RETINOBLASTOMA PROTEIN N-DOMAIN              
TITLE    2 PROVIDES INSIGHT INTO TUMOR SUPPRESSION, LIGAND                      
TITLE    3 INTERACTION AND HOLOPROTEIN ARCHITECTURE                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RETINOBLASTOMA-ASSOCIATED PROTEIN;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN;                                         
COMPND   5 SYNONYM: PP110, P105-RB, RB;                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RB1;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 PLYSS;                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX6P1                                   
KEYWDS    CYCLIN FOLD, CYCLIN WEDGE, ANTITUMOR PROTEIN                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.HASSLER,S.MITTNACHT,L.H.PEARL                                       
REVDAT   2   24-FEB-09 2QDJ    1       VERSN                                    
REVDAT   1   22-JAN-08 2QDJ    0                                                
JRNL        AUTH   M.HASSLER,S.SINGH,W.W.YUE,M.LUCZYNSKI,R.LAKBIR,              
JRNL        AUTH 2 F.SANCHEZ-SANCHEZ,T.BADER,L.H.PEARL,S.MITTNACHT              
JRNL        TITL   CRYSTAL STRUCTURE OF THE RETINOBLASTOMA PROTEIN N            
JRNL        TITL 2 DOMAIN PROVIDES INSIGHT INTO TUMOR SUPPRESSION,              
JRNL        TITL 3 LIGAND INTERACTION, AND HOLOPROTEIN ARCHITECTURE.            
JRNL        REF    MOL.CELL                      V.  28   371 2007              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   17996702                                                     
JRNL        DOI    10.1016/J.MOLCEL.2007.08.023                                 
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 51.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 24550                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.231                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1288                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1778                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 97                           
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2117                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 234                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.50000                                             
REMARK   3    B22 (A**2) : -0.95000                                             
REMARK   3    B33 (A**2) : 1.45000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.184         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.174         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2152 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2901 ; 1.189 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   253 ; 4.792 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    94 ;37.512 ;25.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   416 ;16.890 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;23.965 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   341 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1540 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1170 ; 0.242 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1531 ; 0.326 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   132 ; 0.118 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    48 ; 0.288 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.127 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1295 ; 2.479 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2108 ; 3.421 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   857 ; 3.866 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   793 ; 5.030 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2QDJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043462.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-OCT-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93300                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25840                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 51.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NA ACETATE, 25% (W/V) PEG          
REMARK 280  4000, 0.1 M TRIS, PH 8.0, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z                                         
REMARK 290       7555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       36.14800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       53.32450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       36.14800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       53.32450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       36.14800            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       53.32450            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       36.14800            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       53.32450            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 435  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 477  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 496  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 589  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL A    84                                                      
REMARK 465     ASP A    85                                                      
REMARK 465     GLY A    86                                                      
REMARK 465     VAL A    87                                                      
REMARK 465     LEU A    88                                                      
REMARK 465     GLY A    89                                                      
REMARK 465     GLY A    90                                                      
REMARK 465     TYR A    91                                                      
REMARK 465     ILE A    92                                                      
REMARK 465     GLN A    93                                                      
REMARK 465     GLN A   207                                                      
REMARK 465     MSE A   208                                                      
REMARK 465     GLU A   209                                                      
REMARK 465     PRO A   245                                                      
REMARK 465     ILE A   246                                                      
REMARK 465     ASN A   247                                                      
REMARK 465     GLY A   248                                                      
REMARK 465     SER A   249                                                      
REMARK 465     PRO A   250                                                      
REMARK 465     ARG A   251                                                      
REMARK 465     THR A   252                                                      
REMARK 465     PRO A   253                                                      
REMARK 465     ARG A   254                                                      
REMARK 465     ARG A   255                                                      
REMARK 465     GLY A   256                                                      
REMARK 465     GLN A   257                                                      
REMARK 465     ASN A   258                                                      
REMARK 465     ARG A   259                                                      
REMARK 465     SER A   260                                                      
REMARK 465     ALA A   261                                                      
REMARK 465     ARG A   262                                                      
REMARK 465     ILE A   263                                                      
REMARK 465     ALA A   264                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     GLN A   266                                                      
REMARK 465     LEU A   267                                                      
REMARK 465     GLU A   268                                                      
REMARK 465     ASN A   269                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     LEU A   305                                                      
REMARK 465     VAL A   306                                                      
REMARK 465     THR A   307                                                      
REMARK 465     SER A   308                                                      
REMARK 465     ASN A   309                                                      
REMARK 465     GLY A   310                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A 205    CG1  CG2                                            
REMARK 470     LEU A 206    CG   CD1  CD2                                       
REMARK 470     ASP A 210    CG   OD1  OD2                                       
REMARK 470     ASP A 270    CG   OD1  OD2                                       
REMARK 470     LEU A 303    CG   CD1  CD2                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LEU A  212   N                                                   
REMARK 480     ILE A  214   CD1                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 210   N   -  CA  -  C   ANGL. DEV. = -16.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A 205       48.87   -106.89                                   
REMARK 500    ASP A 211       95.92     64.34                                   
REMARK 500    LYS A 279        4.67    -66.47                                   
REMARK 500    ASN A 295      -57.08   -154.17                                   
REMARK 500    SER A 302       45.48    -62.90                                   
REMARK 500    ASP A 330     -115.24   -101.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2QDJ A   52   355  UNP    P06400   RB_HUMAN        52    355             
SEQADV 2QDJ MSE A  113  UNP  P06400    MET   113 MODIFIED RESIDUE               
SEQADV 2QDJ MSE A  148  UNP  P06400    MET   148 MODIFIED RESIDUE               
SEQADV 2QDJ MSE A  208  UNP  P06400    MET   208 MODIFIED RESIDUE               
SEQADV 2QDJ MSE A  219  UNP  P06400    MET   219 MODIFIED RESIDUE               
SEQADV 2QDJ MSE A  233  UNP  P06400    MET   233 MODIFIED RESIDUE               
SEQADV 2QDJ MSE A  300  UNP  P06400    MET   300 MODIFIED RESIDUE               
SEQRES   1 A  304  THR GLU GLU PRO ASP PHE THR ALA LEU CYS GLN LYS LEU          
SEQRES   2 A  304  LYS ILE PRO ASP HIS VAL ARG GLU ARG ALA TRP LEU THR          
SEQRES   3 A  304  TRP GLU LYS VAL SER SER VAL ASP GLY VAL LEU GLY GLY          
SEQRES   4 A  304  TYR ILE GLN LYS LYS LYS GLU LEU TRP GLY ILE CYS ILE          
SEQRES   5 A  304  PHE ILE ALA ALA VAL ASP LEU ASP GLU MSE SER PHE THR          
SEQRES   6 A  304  PHE THR GLU LEU GLN LYS ASN ILE GLU ILE SER VAL HIS          
SEQRES   7 A  304  LYS PHE PHE ASN LEU LEU LYS GLU ILE ASP THR SER THR          
SEQRES   8 A  304  LYS VAL ASP ASN ALA MSE SER ARG LEU LEU LYS LYS TYR          
SEQRES   9 A  304  ASP VAL LEU PHE ALA LEU PHE SER LYS LEU GLU ARG THR          
SEQRES  10 A  304  CYS GLU LEU ILE TYR LEU THR GLN PRO SER SER SER ILE          
SEQRES  11 A  304  SER THR GLU ILE ASN SER ALA LEU VAL LEU LYS VAL SER          
SEQRES  12 A  304  TRP ILE THR PHE LEU LEU ALA LYS GLY GLU VAL LEU GLN          
SEQRES  13 A  304  MSE GLU ASP ASP LEU VAL ILE SER PHE GLN LEU MSE LEU          
SEQRES  14 A  304  CYS VAL LEU ASP TYR PHE ILE LYS LEU SER PRO PRO MSE          
SEQRES  15 A  304  LEU LEU LYS GLU PRO TYR LYS THR ALA VAL ILE PRO ILE          
SEQRES  16 A  304  ASN GLY SER PRO ARG THR PRO ARG ARG GLY GLN ASN ARG          
SEQRES  17 A  304  SER ALA ARG ILE ALA LYS GLN LEU GLU ASN ASP THR ARG          
SEQRES  18 A  304  ILE ILE GLU VAL LEU CYS LYS GLU HIS GLU CYS ASN ILE          
SEQRES  19 A  304  ASP GLU VAL LYS ASN VAL TYR PHE LYS ASN PHE ILE PRO          
SEQRES  20 A  304  PHE MSE ASN SER LEU GLY LEU VAL THR SER ASN GLY LEU          
SEQRES  21 A  304  PRO GLU VAL GLU ASN LEU SER LYS ARG TYR GLU GLU ILE          
SEQRES  22 A  304  TYR LEU LYS ASN LYS ASP LEU ASP ALA ARG LEU PHE LEU          
SEQRES  23 A  304  ASP HIS ASP LYS THR LEU GLN THR ASP SER ILE ASP SER          
SEQRES  24 A  304  PHE GLU THR GLN ARG                                          
MODRES 2QDJ MSE A  113  MET  SELENOMETHIONINE                                   
MODRES 2QDJ MSE A  148  MET  SELENOMETHIONINE                                   
MODRES 2QDJ MSE A  219  MET  SELENOMETHIONINE                                   
MODRES 2QDJ MSE A  233  MET  SELENOMETHIONINE                                   
MODRES 2QDJ MSE A  300  MET  SELENOMETHIONINE                                   
HET    MSE  A 113       8                                                       
HET    MSE  A 148       8                                                       
HET    MSE  A 219       8                                                       
HET    MSE  A 233       8                                                       
HET    MSE  A 300       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    5(C5 H11 N O2 SE)                                            
FORMUL   2  HOH   *234(H2 O)                                                    
HELIX    1   1 GLU A   54  LEU A   64  1                                  11    
HELIX    2   2 PRO A   67  SER A   83  1                                  17    
HELIX    3   3 LYS A   94  ASP A  111  1                                  18    
HELIX    4   4 THR A  116  GLU A  125  1                                  10    
HELIX    5   5 SER A  127  LYS A  136  1                                  10    
HELIX    6   6 SER A  141  TYR A  173  1                                  33    
HELIX    7   7 SER A  187  VAL A  205  1                                  19    
HELIX    8   8 ASP A  211  LEU A  229  1                                  19    
HELIX    9   9 PRO A  231  LEU A  235  5                                   5    
HELIX   10  10 LYS A  240  ILE A  244  5                                   5    
HELIX   11  11 THR A  271  GLU A  282  1                                  12    
HELIX   12  12 ASN A  284  ASN A  295  1                                  12    
HELIX   13  13 ASN A  295  MSE A  300  1                                   6    
HELIX   14  14 GLU A  313  LYS A  329  1                                  17    
HELIX   15  15 ASP A  332  HIS A  339  5                                   8    
HELIX   16  16 ASP A  340  GLN A  344  5                                   5    
HELIX   17  17 ASP A  346  GLN A  354  1                                   9    
LINK         C   GLU A 112                 N   MSE A 113     1555   1555  1.32  
LINK         C   MSE A 113                 N   SER A 114     1555   1555  1.32  
LINK         C   ALA A 147                 N   MSE A 148     1555   1555  1.33  
LINK         C   MSE A 148                 N   SER A 149     1555   1555  1.33  
LINK         C   LEU A 218                 N   MSE A 219     1555   1555  1.33  
LINK         C   MSE A 219                 N   LEU A 220     1555   1555  1.33  
LINK         C   PRO A 232                 N   MSE A 233     1555   1555  1.33  
LINK         C   MSE A 233                 N   LEU A 234     1555   1555  1.33  
LINK         C   PHE A 299                 N   MSE A 300     1555   1555  1.33  
LINK         C   MSE A 300                 N   ASN A 301     1555   1555  1.33  
CISPEP   1 GLU A  237    PRO A  238          0         5.58                     
CRYST1   72.296  106.649   98.191  90.00  90.00  90.00 C 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013832  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009377  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010184        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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